MolNFT v1 · #160697 · protein
Crystal structure of the carboxyltransferase subunit of acc (ACCD6) in complex with inhibitor quizalofop-P derivative from mycobacterium tuberculosis
6PRW: “Crystal structure of the carboxyltransferase subunit of acc (ACCD6) in complex with inhibitor quizalofop-P…”. X-ray diffraction, 1 ligand (OWD). MolNFT v1 #160697 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6PRW
- Type
- protein
- Length
- 3,376 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A0E7XNZ4
- Ligands
- OWD
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E | — | protein | 426 | — | A0A0E7XNZ4 |
| B, F | — | protein | 424 | — | A0A0E7XNZ4 |
| C, G | — | protein | 410 | — | A0A0E7XNZ4 |
| D, H | — | protein | 428 | — | A0A0E7XNZ4 |
Ligands and binding sites
- OWD · {4-[(6-chloroquinoxalin-2-yl)oxy]phenyl}acetic acid · ligand · 8 copies · chains A, B, C, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6PRW · Crystal structure of the carboxyltransferase subunit of acc (ACCD6) in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A0A0E7XNZ4
- Elsewhere: RCSB PDB 6PRW · PDBe 6PRW · UniProt A0A0E7XNZ4
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